Enhancement of TREK1 channel surface expression by protein-protein interaction with β-COP

Eunju Kim; Eun Mi Hwang; Oleg Yarishkin; Jae Cheal Yoo; Donggyu Kim; Nammi Park; Minhee Cho; Young Sun Lee; Choong Hyun Sun; Gwan Su Yi; Jiyun Yoo; Dawon Kang; Jaehee Han; Seong Geun Hong; Jae Yong Park

doi:10.1016/j.bbrc.2010.03.171

Enhancement of TREK1 channel surface expression by protein-protein interaction with β-COP

Eunju Kim
, Eun Mi Hwang
, Oleg Yarishkin
, Jae Cheal Yoo
, Donggyu Kim
, Nammi Park
, Minhee Cho
, Young Sun Lee
, Choong Hyun Sun
, Gwan Su Yi
, Jiyun Yoo
, Dawon Kang
, Jaehee Han
, Seong Geun Hong
, Jae Yong Park^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

29 Citations (Scopus)

Abstract

TREK1 belongs to a family of two-pore-domain K⁺ (K_2P) channels and produce background currents that regulate cell excitability. In the present study, we identified a vesicle transport protein, β-COP, as an interacting partner by yeast two-hybrid screening of a human brain cDNA library with N-terminal region of TREK1 (TREK1-N) as bait. Several in vitro and in vivo binding assays confirmed the protein-protein interaction between TREK1 and β-COP. We also found that β-COP was associated with TREK1 in native condition at the PC3 cells. When RFP-β-COP was co-transfected with GFP-TREK1 into COS-7 cells, both proteins were found localized to the plasma membrane. In addition, the channel activity and surface expression of GFP-TREK1 increased dramatically by co-transfection with RFP-β-COP. Surface expression of the TREK1 channel was also clearly reduced with the addition of β-COP-specific shRNA. Collectively, these data suggest that β-COP plays a critical role in the forward transport of TREK1 channel to the plasma membrane. Crown

Original language	English
Pages (from-to)	244-250
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	395
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2010.03.171
Publication status	Published - 2010 Apr 30
Externally published	Yes

Keywords

TREK1
Trafficking
Yeast two-hybrid screening
β-COP

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2010.03.171

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Kim, E., Hwang, E. M., Yarishkin, O., Yoo, J. C., Kim, D., Park, N., Cho, M., Lee, Y. S., Sun, C. H., Yi, G. S., Yoo, J., Kang, D., Han, J., Hong, S. G., & Park, J. Y. (2010). Enhancement of TREK1 channel surface expression by protein-protein interaction with β-COP. Biochemical and biophysical research communications, 395(2), 244-250. https://doi.org/10.1016/j.bbrc.2010.03.171

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title = "Enhancement of TREK1 channel surface expression by protein-protein interaction with β-COP",

abstract = "TREK1 belongs to a family of two-pore-domain K+ (K2P) channels and produce background currents that regulate cell excitability. In the present study, we identified a vesicle transport protein, β-COP, as an interacting partner by yeast two-hybrid screening of a human brain cDNA library with N-terminal region of TREK1 (TREK1-N) as bait. Several in vitro and in vivo binding assays confirmed the protein-protein interaction between TREK1 and β-COP. We also found that β-COP was associated with TREK1 in native condition at the PC3 cells. When RFP-β-COP was co-transfected with GFP-TREK1 into COS-7 cells, both proteins were found localized to the plasma membrane. In addition, the channel activity and surface expression of GFP-TREK1 increased dramatically by co-transfection with RFP-β-COP. Surface expression of the TREK1 channel was also clearly reduced with the addition of β-COP-specific shRNA. Collectively, these data suggest that β-COP plays a critical role in the forward transport of TREK1 channel to the plasma membrane. Crown",

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author = "Eunju Kim and Hwang, \{Eun Mi\} and Oleg Yarishkin and Yoo, \{Jae Cheal\} and Donggyu Kim and Nammi Park and Minhee Cho and Lee, \{Young Sun\} and Sun, \{Choong Hyun\} and Yi, \{Gwan Su\} and Jiyun Yoo and Dawon Kang and Jaehee Han and Hong, \{Seong Geun\} and Park, \{Jae Yong\}",

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AU - Kim, Eunju

AU - Hwang, Eun Mi

AU - Yarishkin, Oleg

AU - Yoo, Jae Cheal

AU - Kim, Donggyu

AU - Park, Nammi

AU - Cho, Minhee

AU - Lee, Young Sun

AU - Sun, Choong Hyun

AU - Yi, Gwan Su

AU - Yoo, Jiyun

AU - Kang, Dawon

AU - Han, Jaehee

AU - Hong, Seong Geun

AU - Park, Jae Yong

PY - 2010/4/30

Y1 - 2010/4/30

N2 - TREK1 belongs to a family of two-pore-domain K+ (K2P) channels and produce background currents that regulate cell excitability. In the present study, we identified a vesicle transport protein, β-COP, as an interacting partner by yeast two-hybrid screening of a human brain cDNA library with N-terminal region of TREK1 (TREK1-N) as bait. Several in vitro and in vivo binding assays confirmed the protein-protein interaction between TREK1 and β-COP. We also found that β-COP was associated with TREK1 in native condition at the PC3 cells. When RFP-β-COP was co-transfected with GFP-TREK1 into COS-7 cells, both proteins were found localized to the plasma membrane. In addition, the channel activity and surface expression of GFP-TREK1 increased dramatically by co-transfection with RFP-β-COP. Surface expression of the TREK1 channel was also clearly reduced with the addition of β-COP-specific shRNA. Collectively, these data suggest that β-COP plays a critical role in the forward transport of TREK1 channel to the plasma membrane. Crown

AB - TREK1 belongs to a family of two-pore-domain K+ (K2P) channels and produce background currents that regulate cell excitability. In the present study, we identified a vesicle transport protein, β-COP, as an interacting partner by yeast two-hybrid screening of a human brain cDNA library with N-terminal region of TREK1 (TREK1-N) as bait. Several in vitro and in vivo binding assays confirmed the protein-protein interaction between TREK1 and β-COP. We also found that β-COP was associated with TREK1 in native condition at the PC3 cells. When RFP-β-COP was co-transfected with GFP-TREK1 into COS-7 cells, both proteins were found localized to the plasma membrane. In addition, the channel activity and surface expression of GFP-TREK1 increased dramatically by co-transfection with RFP-β-COP. Surface expression of the TREK1 channel was also clearly reduced with the addition of β-COP-specific shRNA. Collectively, these data suggest that β-COP plays a critical role in the forward transport of TREK1 channel to the plasma membrane. Crown

KW - TREK1

KW - Trafficking

KW - Yeast two-hybrid screening

KW - β-COP

UR - https://www.scopus.com/pages/publications/77951652951

U2 - 10.1016/j.bbrc.2010.03.171

DO - 10.1016/j.bbrc.2010.03.171

M3 - Article

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AN - SCOPUS:77951652951

SN - 0006-291X

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JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 2

ER -

Enhancement of TREK1 channel surface expression by protein-protein interaction with β-COP

Abstract

Keywords

ASJC Scopus subject areas

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